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2BPI

Structure of Iron dependent superoxide dismutase from P. falciparum.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006801biological_processsuperoxide metabolic process
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0046872molecular_functionmetal ion binding
B0004784molecular_functionsuperoxide dismutase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006801biological_processsuperoxide metabolic process
B0006979biological_processresponse to oxidative stress
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 1198
ChainResidue
AHIS26
AHIS73
AASP157
AHIS161
AHOH2055

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 1198
ChainResidue
BHOH2054
BHIS26
BHIS73
BASP157
BHIS161

Functional Information from PROSITE/UniProt
site_idPS00088
Number of Residues8
DetailsSOD_MN Manganese and iron superoxide dismutases signature. DiWEHAYY
ChainResidueDetails
AASP157-TYR164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AHIS26
AHIS73
AASP157
AHIS161
BHIS26
BHIS73
BASP157
BHIS161

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PDB entries from 2024-07-24

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